dc.contributor.advisor | Neher, Erwin Prof. Dr. | de |
dc.contributor.author | Rah, Jong-Cheol | de |
dc.date.accessioned | 2004-12-16T12:11:58Z | de |
dc.date.accessioned | 2013-01-18T14:29:27Z | de |
dc.date.available | 2013-01-30T23:51:13Z | de |
dc.date.issued | 2004-12-16 | de |
dc.identifier.uri | http://hdl.handle.net/11858/00-1735-0000-0006-B6B4-F | de |
dc.identifier.uri | http://dx.doi.org/10.53846/goediss-3315 | |
dc.description.abstract | During vesicle priming at the central synapse,
Syntaxin 1, together with SNAP25 and Synaptobrevin,
assemble into the synaptic SNARE complex. The formation
of SNARE complex is thought to provide the energy
needed that enables vesicle exocytosis during Ca2+
triggering step at the presynapse. Among the SNARE
proteins, Syntaxin 1 is thought to play a special role
in regulating the rate of SNARE assembly by adopting
two conformations; a closed autoinhibitory conformation
in which core complex domain is hindered by N-terminal
Habc domain, and an open conformation in which the
SNARE motif of syntaxin is open and ready to interact
with the other SNAREs.In the present study we examined the role of the
conformational switch of syntaxin 1 by analyzing
synaptic properties of genetically modified mice
expressing a mutation that leaves syntaxin 1 in a
constitutively open conformation. In cultured
hippocampal neurons, the mutation led to a significant
increase in the rate of vesicle priming, supporting the
hypothesis that syntaxin 1 regulates vesicle priming
during the SNARE complex assembly process.
Surprisingly, we also found that the mutation led to an
increase in synaptic release probability, suggesting
that the conformation of syntaxin 1 also regulates
vesicle fusion by reducing the energy barrier of
vesicle fusion to the plasma membrane. Our data support
the idea that the SNARE complex member syntaxin 1 and
its individual conformations are crucial regulators of
the efficacy and short-term plasticity of synaptic
transmission. | de |
dc.format.mimetype | application/pdf | de |
dc.language.iso | eng | de |
dc.rights.uri | http://webdoc.sub.gwdg.de/diss/copyr_diss.html | de |
dc.title | The Regulatory Role of Syntaxin 1 N-terminal Conformation in Vesicle Priming and Exocytosis | de |
dc.type | doctoralThesis | de |
dc.title.translated | Die Regulation der Vesikelreifung und -Freisetzung durch Syntaxin 1 | de |
dc.contributor.referee | Gradmann, Dietrich Prof. Dr. | de |
dc.date.examination | 2004-11-02 | de |
dc.subject.dnb | 590 Tiere (Zoologie) | de |
dc.description.abstracteng | During vesicle priming at the central synapse,
Syntaxin 1, together with SNAP25 and Synaptobrevin,
assemble into the synaptic SNARE complex. The formation
of SNARE complex is thought to provide the energy
needed that enables vesicle exocytosis during Ca2+
triggering step at the presynapse. Among the SNARE
proteins, Syntaxin 1 is thought to play a special role
in regulating the rate of SNARE assembly by adopting
two conformations; a closed autoinhibitory conformation
in which core complex domain is hindered by N-terminal
Habc domain, and an open conformation in which the
SNARE motif of syntaxin is open and ready to interact
with the other SNAREs.In the present study we examined the role of the
conformational switch of syntaxin 1 by analyzing
synaptic properties of genetically modified mice
expressing a mutation that leaves syntaxin 1 in a
constitutively open conformation. In cultured
hippocampal neurons, the mutation led to a significant
increase in the rate of vesicle priming, supporting the
hypothesis that syntaxin 1 regulates vesicle priming
during the SNARE complex assembly process.
Surprisingly, we also found that the mutation led to an
increase in synaptic release probability, suggesting
that the conformation of syntaxin 1 also regulates
vesicle fusion by reducing the energy barrier of
vesicle fusion to the plasma membrane. Our data support
the idea that the SNARE complex member syntaxin 1 and
its individual conformations are crucial regulators of
the efficacy and short-term plasticity of synaptic
transmission. | de |
dc.contributor.coReferee | Wimmer, Ernst A. Prof. Dr. | de |
dc.contributor.thirdReferee | Fritz, Hans-Joachim Prof. Dr. | de |
dc.subject.topic | Mathematics and Computer Science | de |
dc.subject.ger | hippocampus | de |
dc.subject.ger | CNS | de |
dc.subject.ger | neuron | de |
dc.subject.ger | neurotransmitter | de |
dc.subject.ger | exocytosis | de |
dc.subject.ger | SNARE | de |
dc.subject.ger | syntaxin 1A | de |
dc.subject.ger | conformation | de |
dc.subject.eng | hippocampus | de |
dc.subject.eng | CNS | de |
dc.subject.eng | neuron | de |
dc.subject.eng | neurotransmitter | de |
dc.subject.eng | exocytosis | de |
dc.subject.eng | SNARE | de |
dc.subject.eng | syntaxin 1A | de |
dc.subject.eng | conformation | de |
dc.subject.bk | 42.12 | de |
dc.identifier.urn | urn:nbn:de:gbv:7-webdoc-316-1 | de |
dc.identifier.purl | webdoc-316 | de |
dc.affiliation.institute | Göttinger Graduiertenschule für Neurowissenschaften und molekulare Biowissenschaften (GGNB) | de |
dc.identifier.ppn | 487823125 | de |